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Database: UniProt
Entry: K0VNK5_MYCVA
LinkDB: K0VNK5_MYCVA
Original site: K0VNK5_MYCVA 
ID   K0VNK5_MYCVA            Unreviewed;       361 AA.
AC   K0VNK5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:EJZ12789.1};
GN   ORFNames=MVAC_01865 {ECO:0000313|EMBL:EJZ12789.1};
OS   Mycolicibacterium vaccae ATCC 25954.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ12789.1, ECO:0000313|Proteomes:UP000006072};
RN   [1] {ECO:0000313|EMBL:EJZ12789.1, ECO:0000313|Proteomes:UP000006072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ12789.1,
RC   ECO:0000313|Proteomes:UP000006072};
RX   PubMed=23105074; DOI=10.1128/JB.01462-12;
RA   Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA   Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT   "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL   J. Bacteriol. 194:6339-6340(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJZ12789.1}.
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DR   EMBL; ALQA01000002; EJZ12789.1; -; Genomic_DNA.
DR   RefSeq; WP_003928326.1; NZ_JH814683.1.
DR   AlphaFoldDB; K0VNK5; -.
DR   PATRIC; fig|1194972.3.peg.382; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_1_0_11; -.
DR   Proteomes; UP000006072; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:EJZ12789.1}.
FT   DOMAIN          43..314
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   361 AA;  39976 MW;  2F128E199B371EB1 CRC64;
     MAGRSALSEF GEPIQLVAPD GAPTPEARYR RDLPPETLAW LYECMVLTRE IDTEFVNLQR
     QGELALFASC RGQEAAQVGA AACLRKTDWL FPQYRELGAF LLRAIAPAQL GALWRGRWHG
     GLGFTDKCVA PVSIPIGTHG LHAVGAAMAA RQLGEDSVTV AFLGDGATSE GDAHEALNLA
     AVFRAPCVFF VQNNQWAISV PVERQHAGPT LAHRAIGYGM PGVRVDGNDV LACYAVMEQA
     AARAREGGGP TFIEAVTYRM GPHTTSDDPT RYRPAEDVER WRARDPITRY RTYLQRGEVW
     TQRLEERIAH RAQRMRSELR DAVINEPDID IVEVFDTVYH DITPDLARQR DELLAELAKE
     S
//
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